MA7D3_HUMAN
ID MA7D3_HUMAN Reviewed; 876 AA.
AC Q8IWC1; A2A2J0; A6NCZ7; A6NHR4; B4DWD2; H7BY77; Q5JXI5; Q5JXI6; Q6P2S1;
AC Q9H9M8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=MAP7 domain-containing protein 3;
GN Name=MAP7D3; Synonyms=MDP3 {ECO:0000303|PubMed:22142902};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 701-876 (ISOFORMS 1/2/3).
RC TISSUE=Synovium, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ALA-502 AND ARG-628.
RC TISSUE=Brain, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15561729; DOI=10.1074/mcp.m400158-mcp200;
RA Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.;
RT "Proteome analysis of the human mitotic spindle.";
RL Mol. Cell. Proteomics 4:35-43(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-457; SER-461 AND
RP SER-524, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, INTERACTION WITH MICROTUBULES AND TUBULIN, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22142902; DOI=10.4161/cc.10.22.18106;
RA Sun X., Shi X., Liu M., Li D., Zhang L., Liu X., Zhou J.;
RT "Mdp3 is a novel microtubule-binding protein that regulates microtubule
RT assembly and stability.";
RL Cell Cycle 10:3929-3937(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-441; SER-461;
RP SER-490; SER-817 AND SER-832, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH MICROTUBULES AND TUBULIN, AND FUNCTION.
RX PubMed=24927501; DOI=10.1371/journal.pone.0099539;
RA Yadav S., Verma P.J., Panda D.;
RT "C-terminal region of MAP7 domain containing protein 3 (MAP7D3) promotes
RT microtubule polymerization by binding at the C-terminal tail of tubulin.";
RL PLoS ONE 9:E99539-E99539(2014).
RN [17]
RP VARIANT ARG-561.
RX PubMed=26506222; DOI=10.1002/ana.24550;
RA Park H.J., Hong Y.B., Choi Y.C., Lee J., Kim E.J., Lee J.S., Mo W.M.,
RA Ki S.M., Kim H.I., Kim H.J., Hyun Y.S., Hong H.D., Nam K., Jung S.C.,
RA Kim S.B., Kim S.H., Kim D.H., Oh K.W., Kim S.H., Yoo J.H., Lee J.E.,
RA Chung K.W., Choi B.O.;
RT "ADSSL1 mutation relevant to autosomal recessive adolescent onset distal
RT myopathy.";
RL Ann. Neurol. 79:231-243(2016).
CC -!- FUNCTION: Promotes the assembly and stability of microtubules.
CC {ECO:0000269|PubMed:22142902, ECO:0000269|PubMed:24927501}.
CC -!- SUBUNIT: Interacts (via N-terminus coiled coil domains) with tubulin
CC and microtubules. {ECO:0000269|PubMed:22142902,
CC ECO:0000269|PubMed:24927501}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15561729}. Note=Localizes to the microtubules
CC throughout mitosis. {ECO:0000269|PubMed:22142902}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8IWC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWC1-2; Sequence=VSP_028499;
CC Name=3;
CC IsoId=Q8IWC1-3; Sequence=VSP_028498;
CC Name=4;
CC IsoId=Q8IWC1-4; Sequence=VSP_045008;
CC -!- INDUCTION: Expression is cell cycle dependent with the highest levels
CC during G1, S, and M phases, and low level in G2 phase.
CC {ECO:0000269|PubMed:22142902}.
CC -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64350.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK022711; BAB14195.1; -; mRNA.
DR EMBL; AK301478; BAG62994.1; -; mRNA.
DR EMBL; AL832120; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL078638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471150; EAW88475.1; -; Genomic_DNA.
DR EMBL; BC040518; AAH40518.1; -; mRNA.
DR EMBL; BC064350; AAH64350.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44004.1; -. [Q8IWC1-1]
DR CCDS; CCDS55508.1; -. [Q8IWC1-3]
DR CCDS; CCDS55509.1; -. [Q8IWC1-4]
DR RefSeq; NP_001166987.1; NM_001173516.1. [Q8IWC1-4]
DR RefSeq; NP_001166988.1; NM_001173517.1. [Q8IWC1-3]
DR RefSeq; NP_078873.2; NM_024597.3. [Q8IWC1-1]
DR AlphaFoldDB; Q8IWC1; -.
DR SMR; Q8IWC1; -.
DR BioGRID; 122777; 87.
DR IntAct; Q8IWC1; 41.
DR MINT; Q8IWC1; -.
DR STRING; 9606.ENSP00000318086; -.
DR GlyGen; Q8IWC1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IWC1; -.
DR PhosphoSitePlus; Q8IWC1; -.
DR BioMuta; MAP7D3; -.
DR DMDM; 158705880; -.
DR EPD; Q8IWC1; -.
DR jPOST; Q8IWC1; -.
DR MassIVE; Q8IWC1; -.
DR MaxQB; Q8IWC1; -.
DR PaxDb; Q8IWC1; -.
DR PeptideAtlas; Q8IWC1; -.
DR PRIDE; Q8IWC1; -.
DR ProteomicsDB; 43531; -.
DR ProteomicsDB; 70842; -. [Q8IWC1-1]
DR ProteomicsDB; 70843; -. [Q8IWC1-2]
DR ProteomicsDB; 70844; -. [Q8IWC1-3]
DR Antibodypedia; 51701; 20 antibodies from 10 providers.
DR DNASU; 79649; -.
DR Ensembl; ENST00000316077.14; ENSP00000318086.9; ENSG00000129680.16. [Q8IWC1-1]
DR Ensembl; ENST00000370661.5; ENSP00000359695.1; ENSG00000129680.16. [Q8IWC1-3]
DR Ensembl; ENST00000370663.9; ENSP00000359697.5; ENSG00000129680.16. [Q8IWC1-4]
DR GeneID; 79649; -.
DR KEGG; hsa:79649; -.
DR MANE-Select; ENST00000316077.14; ENSP00000318086.9; NM_024597.4; NP_078873.2.
DR UCSC; uc004ezs.4; human. [Q8IWC1-1]
DR CTD; 79649; -.
DR DisGeNET; 79649; -.
DR GeneCards; MAP7D3; -.
DR HGNC; HGNC:25742; MAP7D3.
DR HPA; ENSG00000129680; Low tissue specificity.
DR MIM; 300930; gene.
DR neXtProt; NX_Q8IWC1; -.
DR OpenTargets; ENSG00000129680; -.
DR PharmGKB; PA162394972; -.
DR VEuPathDB; HostDB:ENSG00000129680; -.
DR eggNOG; ENOG502SDH7; Eukaryota.
DR GeneTree; ENSGT00950000182941; -.
DR InParanoid; Q8IWC1; -.
DR OMA; WSWEGSA; -.
DR OrthoDB; 441248at2759; -.
DR PhylomeDB; Q8IWC1; -.
DR TreeFam; TF332273; -.
DR PathwayCommons; Q8IWC1; -.
DR SignaLink; Q8IWC1; -.
DR BioGRID-ORCS; 79649; 13 hits in 708 CRISPR screens.
DR ChiTaRS; MAP7D3; human.
DR GenomeRNAi; 79649; -.
DR Pharos; Q8IWC1; Tbio.
DR PRO; PR:Q8IWC1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8IWC1; protein.
DR Bgee; ENSG00000129680; Expressed in calcaneal tendon and 125 other tissues.
DR ExpressionAtlas; Q8IWC1; baseline and differential.
DR Genevisible; Q8IWC1; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA:UniProtKB.
DR InterPro; IPR008604; MAP7_fam.
DR Pfam; PF05672; MAP7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..876
FT /note="MAP7 domain-containing protein 3"
FT /id="PRO_0000306812"
FT REGION 72..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..144
FT /evidence="ECO:0000255"
FT COILED 558..640
FT /evidence="ECO:0000255"
FT COILED 689..724
FT /evidence="ECO:0000255"
FT COMPBIAS 170..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..23
FT /note="MMADGAAAGAGGSPSLRELRARM -> MTSPR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045008"
FT VAR_SEQ 179..214
FT /note="ANKRSASTEKLEQGTSALIRQMPLSSAGLQNSVAKR -> G (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028498"
FT VAR_SEQ 246..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028499"
FT VARIANT 502
FT /note="E -> A (in dbSNP:rs1055497)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035314"
FT VARIANT 561
FT /note="K -> R (in dbSNP:rs748582851)"
FT /evidence="ECO:0000269|PubMed:26506222"
FT /id="VAR_077003"
FT VARIANT 628
FT /note="Q -> R (in dbSNP:rs2273221)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035315"
FT CONFLICT 71
FT /note="L -> S (in Ref. 1; BAG62994)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="K -> R (in Ref. 1; BAG62994)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="A -> T (in Ref. 5; AAH40518)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="R -> Q (in Ref. 2; AL832120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 876 AA; 98429 MW; C149899FB0002B39 CRC64;
MMADGAAAGA GGSPSLRELR ARMVAAANEI AKERRKQDVV NRVATHSSNI RSTFKPVIDG
SMLKNDIKQR LARERREEKR RQQDANKETQ LLEKERKTKL QYEKQMEERQ RKLKERKEKE
EQRRIAAEEK RHQKDEAQKE KFTAILYRTL ERRRLADDYQ QKRWSWGGSA MANSESKTAN
KRSASTEKLE QGTSALIRQM PLSSAGLQNS VAKRKTDKER SSSLNRRDSN LHSSTDKEQA
ERKPRVTGVT NYVMQYVTVP LRKCTSDELR AVMFPMSTMK IPPQTKVEES PLEKVETPPK
ASVDAPPQVN VEVFCNTSME ASPKAGVGMA PEVSTDSFPV VSVDVSPVVS TYDSEMSMDA
SPELSIEALP KVDLETVPKV SIVASPEASL EAPPEVSLEA LPEVSVEAAP EGSLEAPPKG
SAEVAPKESV KGSPKESMEA SPEAMVKASP KTSLEASMEA SPKAKARDAP KKSEMDKQAL
IPIAKKRLSS YTECYKWSSS PENACGLPSP ISTNRQIQKN CPPSPLPLIS KQSPQTSFPY
KIMPIQHTLS VQSASSTVKK KKETVSKTTN RCEALSQRHM IYEESGNKST AGIMNAEAAT
KILTELRRLA REQREKEEEE RQREEMQQRV IKKSKDMAKE AVGGQAEDHL KLKDGQQQNE
TKKKKGWLDQ EDQEAPLQKG DAKIKAQEEA DKRKKEHERI MLQNLQERLE RKKRIEEIMK
RTRKTDVNAS KVTETSSHDI YEEAEADNEE SDKDSLNEMF PSAILNGTGS PTKFKMPFNN
AKKMTHKLVF LEDGTSQVRK EPKTYFNGDL KNFRQKSMKD TSIQEVVSRP SSKRMTSHTT
KTRKADETNT TSRSSAQTKS EGFHDILPKS SDTFRQ
